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Methionine, sulfur-containing amino acid gotten by the hydrolysis of most typical proteins. Initially separated from casein (1922 ), methionine accounts for about 5 percent of the weight of egg albumin; other proteins include much smaller quantities of methionine. It is one of several so-called vital amino acids for mammals and fowl; i.e., they can not synthesize it. In bacteria it is manufactured from the amino acids cysteine and aspartic acid.

Methionine is essential in methylation (the procedure by which methyl, or -ch3, groups are contributed to compounds) and is also a precursor of two other amino acids, cystine and cysteine. [1]

Other names

Methionine; methionine, l-; γ-methylthio-α-aminobutyric acid; butanoic acid, 2-amino-4-( methylthio)-, (s)-; cymethion; l-(-)- methionine; met; s-methionine; 2-amino-4-( methylthio) butyric acid; butyric acid, 2-amino-4-( methylthio)-; l(-)- amino-γ-methylthiobutyric acid; l-α-amino-γ-methylmercaptobutyric acid; l-γ-methylthio-α-aminobutyric acid; 2-amino-4-methylthiobutanoic acid; liquimeth; acimethin; l-2-amino-4-( methylthio) butyric acid; (s) -2- amino-4-( methylthio) butanoic acid; h-met-oh; l-homocysteine, s-methyl-; nsc 22946; 2-amino-4-methylthiobutanoic acid (s)-. [2]


Methionine is an amino acid. Amino acids are the foundation that our bodies utilize to make proteins. Methionine is found in meat, fish, and dairy items. It plays a crucial role in the many functions within the body.

Methionine is typically taken by mouth to deal with liver conditions and viral infections in addition to lots of other uses. But there is restricted clinical research that supports these usages. [3]


L-methionine, the primary sulfur-containing amino acid in proteins, plays important roles in cell physiology as an antioxidant and in the breakdown of fats and heavy metals. Previous research studies suggesting using l-methionine as a treatment for depression and other diseases suggest that it may also enhance memory and propose a function in brain function. However, some proof shows that an excess of methionine can be hazardous and can increase the danger of developing type-2 diabetes, heart problem, certain kinds of cancer, brain modifications such as schizophrenia, and memory disability. [4]


As an essential amino acid, methionine is not manufactured de novo in humans and other animals, which need to consume methionine or methionine-containing proteins. In plants and bacteria, methionine biosynthesis belongs to the aspartate family, together with threonine and lysine (through diaminopimelate, however not through α-aminoadipate). The main backbone is derived from aspartic acid, while the sulfur might originate from cysteine, methanethiol, or hydrogen sulfide.

First, aspartic acid is transformed via β-aspartyl-semialdehyde into homoserine by 2 decrease actions of the terminal carboxyl group (homoserine has therefore a γ-hydroxyl, hence the homo- series). The intermediate aspartate-semialdehyde is the branching point with the lysine biosynthetic pathway, where it is instead condensed with pyruvate. Homoserine is the branching point with the threonine path, where rather it is isomerised after activating the terminal hydroxyl with phosphate (likewise used for methionine biosynthesis in plants).

Homoserine is then triggered with a phosphate, succinyl or an acetyl group on the hydroxyl.

In plants and potentially in some bacteria, phosphate is used. This action is shared with threonine biosynthesis.

In a lot of organisms, an acetyl group is utilized to activate the homoserine. This can be catalysed in bacteria by an enzyme encoded by metx or meta (not homologues). In enterobacteria and a restricted number of other organisms, succinate is used. The enzyme that catalyses the reaction is meta and the specificity for acetyl-coa and succinyl-coa is determined by a single residue. The physiological basis for the preference of acetyl-coa or succinyl-coa is unknown, but such alternative routes are present in some other pathways (e.g. Lysine biosynthesis and arginine biosynthesis).

The hydroxyl triggering group is then changed with cysteine, methanethiol, or hydrogen sulfide. A replacement reaction is technically a γ-elimination followed by a variation of a michael addition. All the enzymes included are homologues and members of the cys/met metabolism plp-dependent enzyme family, which is a subset of the plp-dependent fold type i clade. They use the cofactor plp (pyridoxal phosphate), which functions by stabilising carbanion intermediates.

If it reacts with cysteine, it produces cystathionine, which is cleaved to yield homocysteine. The enzymes involved are cystathionine-γ-synthase (encoded by metb in bacteria) and cystathionine-β-lyase (metc). Cystathionine is bound differently in the two enzymes enabling β or γ reactions to happen. If it responds with totally free hydrogen sulfide, it produces homocysteine. This is catalysed by o-acetylhomoserine aminocarboxypropyltransferase (previously referred to as o-acetylhomoserine (thiol)- lyase. It is encoded by either mety or metz in bacteria. If it reacts with methanethiol, it produces methionine directly. Methanethiol is a by-product of catabolic path of specific substances, therefore this route is more uncommon. If homocysteine is produced, the thiol group is methylated, yielding methionine. Two methionine synthases are known; one is cobalamin (vitamin b12) reliant and one is independent.

The path utilizing cysteine is called the “transsulfuration pathway”, while the path using hydrogen sulfide (or methanethiol) is called “direct-sulfurylation pathway”.

Cysteine is likewise produced, particularly it can be made from an activated serine and either from homocysteine (” reverse trans-sulfurylation path”) or from hydrogen sulfide (” direct sulfurylation path”); the triggered serine is normally o-acetyl-serine (by means of cysk or cysm in e. Coli), however in aeropyrum pernix and some other archaea o-phosphoserine is used. Cysk and cysm are homologues, however come from the plp fold type iii clade. [5]

System of action

The system of the possible anti-hepatotoxic activity of l-methionine is not entirely clear. It is thought that metabolism of high dosages of acetaminophen in the liver result in reduced levels of hepatic glutathione and increased oxidative stress. L-methionine is a precursor to l-cysteine. L-cysteine itself may have antioxidant activity. L-cysteine is also a precursor to the antioxidant glutathione. Antioxidant activity of l-methionine and metabolites of l-methionine appear to account for its possible anti-hepatotoxic activity. Current research recommends that methionine itself has free-radical scavenging activity by virtue of its sulfur, as well as its chelating ability. [6]

Dietary sources

The met-content of proteins differs significantly depending on the food source. Foods with an especially high portion consist of eggs (31 mg/g protein), cod (30 mg/g), and chicken (28 mg/g). Intermediate material remains in beef (26 mg/g), pork (26 mg/g), milk (25 mg/g), and rice (24 mg/g). Grains and other plant-derived protein sources tend to include a lower portion. Examples are corn (21 mg/g), wheat and oats (18 mg/g), rye and beans (15 mg/g), and cauliflower (14 mg/g). Cooking foods at heats (browning) can reduce fulfilled bioavailability due to oxidation (dworschak, 1980).

Since fulfilled can not be synthesized in the body, adequate quantities have to be supplied. Met and cys are closely linked metabolically, and suggestions are typically provided for the amount of both sulfur amino acids (saa), therefore. Healthy adults ought to get at least 13 mg/kg per day in combination. [7]

What is methionine utilized for?

The sulfur in methionine provides the body with numerous possible health benefits.

these might consist of:.

  • Nurturing the hair, skin, and nails
  • Securing the cells from contaminants
  • Facilitating the cleansing process
  • Slowing down the aging procedure
  • Assisting with the absorption of other nutrients (such as selenium and zinc)
  • Helping in the excretion of heavy metals (such as lead and mercury) assisting the body’s excretion process
  • Preventing excess fat accumulation in the liver (by serving as a lipotropic agent– one that facilitates the breakdown of fats)
  • Reducing cholesterol levels by increasing lecithin production in the liver

Tylenol (acetaminophen) overdose

Taking an oral (by mouth) dose of methionine within 10 hours of tylenol (acetaminophen) overdose has actually been utilized in dealing with acetaminophen poisoning.2 methionine is believed to prevent the byproducts of acetaminophen from harming the liver as a result of an overdose of tylenol. However, other treatments are likewise used and methionine might not be the most effective.


Although a few of the research is combined concerning colon cancer and methionine, a 2013 meta-analysis reports, “this meta-analysis suggests that dietary methionine consumption might be connected with decreased threat of colorectal cancer, specifically colon cancer. More potential research studies with long follow-up time are required to validate these findings.” for instance, a 2016 study reported “amongst the 10 vital amino acids tested, methionine deprivation elicited the greatest repressive effects on the migration and intrusion of these [breast] cancer cells.”.

Some research studies show that a low methionine diet could be helpful. There are specific types of cancer cells that depend upon methionine to grow. Thus, limiting the intake of foods including methionine is helpful for those who have some types of cancer, because it results in the death of the cancer cells.

Alzheimer’s disease

Research studies recommend that l-methionine might help to improve memory and brain function, but according to a research study published by molecular neurodegeneration, “some proof suggests that an excess of methionine can be damaging and can increase the risk of developing type-2 diabetes, heart problem, particular types of cancer, brain changes such as schizophrenia, and memory impairment.”.

Research study on l-methionine and alzheimer’s illness has actually only been carried out in animal studies. In a 2015 mouse model research study found that a diet enhanced with l-methionine led to:.

  • An increase in amyloid (a compound that typically develops in the brains of those with alzheimer’s illness)
  • A rise in the level of tau protein in the brain (an increase can result in tau protein misfolding and clumping together to form abnormal tau tangles, discovered in those with alzheimer’s)
  • A boost in oxidative tension and inflammatory reaction (both believed to raise the risk of alzheimer’s disease)
  • Memory problems and memory loss

The study authors concluded, “taken together, the results of our study show that an l-methionine-enriched diet plan causes impacts in [happening in a living organism] and may contribute to the look of alzheimer’s- like disease in wild-type animals.”.

Other uses

Methionine is frequently taken for other conditions, however there is a lack of scientific research study results to back up the security and effectiveness of its use in these conditions:.

  • Herpes simplex and herpes zoster (shingles)
  • Symptoms of menopause
  • Swelling of the pancreas
  • Liver issues
  • Anxiety
  • Alcoholism
  • Urinary tract infections (uti’s)
  • Asthma and allergic reactions
  • Schizophrenia [8]

It can produce molecules critical for regular cell function

Among the significant functions of methionine in the body is that it can be used to produce other important particles.

It is involved in the production of cysteine, the other sulfur-containing amino acid utilized to construct proteins in the body.

Cysteine can, in turn, develop a range of molecules, consisting of proteins, glutathione and taurine.

Glutathione is often called the “master anti-oxidant” due to its important role in the defenses of your body.

It also contributes in the metabolism of nutrients in the body and the production of dna and proteins.

Taurine has numerous functions that help maintain the health and correct functioning of your cells.

Among the most important particles methionine can be converted into is s-adenosylmethionine, or “sam”.

Sam participates in several chemical reactions by moving part of itself to other molecules, consisting of dna and proteins.

Sam is also utilized in the production of creatine, an important particle for cellular energy.

In general, methionine is straight or indirectly involved in many crucial processes in the body because of the particles it can become.

Methionine can convert into several sulfur-containing molecules with crucial functions, such as glutathione, taurine, sam and creatine. These particles are crucial for the regular functions of the cells in your body.

It plays a role in DNA methylation

Your dna contains the info that makes you who you are.

While much of this details may stay the same for your whole life, environmental aspects can actually alter some aspects of your dna.

This is one of the most intriguing functions of methionine– that it can convert into a molecule called sam. Sam can change your dna by including a methyl group (a carbon atom and its connected hydrogen atoms) to it.

The quantity of methionine in your diet plan might affect how much of this procedure occurs, however there are lots of unanswered questions about this.

It is possible that increasing methionine in the diet might either increase or reduce how much your dna modifications as a result of sa.

Additionally, if these changes occur, they could be advantageous sometimes but destructive in others.

For example, some research study has shown that diets greater in nutrients that include methyl groups to your dna might reduce danger of colorectal cancer.

Nevertheless, other research has revealed that greater methionine consumption could worsen conditions like schizophrenia, maybe due to including more methyl groups to dna.

One of the molecules produced by methionine, sam, can change your dna. It isn’t fully clear how the methionine content of your diet affects this procedure, and it is possible that this process is helpful in some cases and detrimental in others. [9]

Methionine metabolism disorders

There are numerous conditions of methionine and sulfur metabolism in addition to numerous other amino acid and organic acid metabolic process conditions.

Homocysteine is an intermediate in methionine metabolic process; it is either remethylated to regrow methionine or combined with serine in a series of transsulfuration responses to form cystathionine and then cysteine. Cysteine is then metabolized to sulfite, taurine, and glutathione. Different defects in remethylation or transsulfuration can cause homocysteine to collect, resulting in illness.

The initial step in methionine metabolism is its conversion to adenosylmethionine; this conversion requires the enzyme methionine adenosyltransferase. Shortage of this enzyme leads to methionine elevation, which is not scientifically significant except that it triggers false-positive neonatal screening results for homocystinuria.

Traditional homocystinuria

This disorder is brought on by an autosomal recessive shortage of cystathionine beta-synthase, which catalyzes cystathionine formation from homocysteine and serine. Homocysteine builds up and dimerizes to form the disulfide homocystine, which is excreted in the urine. Due to the fact that remethylation is undamaged, a few of the extra homocysteine is transformed to methionine, which accumulates in the blood. Excess homocysteine inclines to thrombosis and has adverse results on connective tissue (possibly including fibrillin), especially the eyes and skeleton; negative neurologic impacts might be because of thrombosis or a direct result.

Arterial and venous thromboembolic phenomena can occur at any age. Many clients develop ectopia lentis (lens subluxation), intellectual special needs, and osteoporosis. Clients can have a marfanoid habitus although they are not generally high.

Diagnosis of traditional homocystinuria is by neonatal screening for raised serum methionine; elevated overall plasma homocysteine levels and/or dna testing are confirmatory. Enzymatic assay in skin fibroblasts can also be done.

Treatment of timeless homocystinuria is a low-methionine diet and l-cysteine supplements integrated with high-dose pyridoxine (a cystathionine synthetase cofactor) 100 to 500 mg orally once a day. Because about half of patients react to high-dose pyridoxine alone, some clinicians do not limit methionine consumption in these clients. Betaine (trimethylglycine), which improves remethylation, can likewise help lower homocysteine. Betaine dosage is normally begun at 100 to 125 mg/kg orally 2 times a day and titrated based upon homocysteine levels; requirements vary extensively, in some cases ≥ 9 g/day is required. Folate 1 to 5 mg orally once a day is likewise given. With early treatment, intellectual result is normal or near normal. Vitamin c, 100 mg orally once a day, may likewise be offered to assist prevent thromboembolism.

Other forms of homocystinuria

Various defects in the remethylation procedure can lead to homocystinuria. Flaws include deficiencies of methionine synthase (ms) and ms reductase (msr), delivery of methylcobalamin and adenosylcobalamin, and shortage of methylenetetrahydrofolate reductase (mthfr, which is required to generate the 5-methyltetrahydrofolate required for the ms reaction). Since there is no methionine elevation in these kinds of homocystinuria, they are not spotted by neonatal screening.

Scientific manifestations resemble other kinds of homocystinuria. In addition, ms and msr shortages are accompanied by neurologic deficits and megaloblastic anemia. Scientific symptom of mthfr deficiency is variable, consisting of intellectual disability, psychosis, weakness, ataxia, and spasticity.

Medical diagnosis of ms and msr shortages is suggested by homocystinuria and megaloblastic anemia and validated by dna testing. Clients with cobalamin problems have megaloblastic anemia and methylmalonic acidemia. Mthfr shortage is identified by dna screening.

Treatment is by replacement of hydroxycobalamin 1 mg im once a day (for clients with ms, msr, and cobalamin defects) and folate in supplements comparable to characteristic homocystinuria.


This condition is brought on by shortage of cystathionase, which transforms cystathionine to cysteine. Cystathionine build-up results in increased urinary excretion but no medical symptoms.

Sulfite oxidase shortage

Sulfite oxidase transforms sulfite to sulfate in the last step of cysteine and methionine degradation; it needs a molybdenum cofactor. Deficiency of either the enzyme or the cofactor causes similar disease; inheritance for both is autosomal recessive.

In its most severe kind, medical symptoms appear in neonates and consist of seizures, hypotonia, and myoclonus, progressing to early death. Patients with milder types might provide likewise to spastic paralysis and may have choreiform movements.

Diagnosis of sulfite oxidase deficiency is recommended by elevated urinary sulfite and validated by determining enzyme levels in fibroblasts and cofactor levels in liver biopsy specimens and/or genetic testing. Treatment of sulfite oxidase deficiency is encouraging. [10]


The following doses have been studied in clinical research study:.

By mouth

For acetaminophen (tylenol) poisoning: 2.5 grams of methionine every 4 hours for 4 doses to prevent liver damage and death. Methionine must be given within 10 hours of taking the acetaminophen. This should be done by a healthcare professional. [11]

Methionine in the body

The estimated average requirement of grownups for total sulphur amino acids (methionine and cysteine) is 15 mg per kg bodyweight and day (kg − 1d − 1). Suggestions for methionine intake are confused by enzyme cofactors and substrates such as vitamin b6, vitamin b9 (folate), vitamin b12, choline, betaine, and creatine. These nutrients enable efficient use of methionine– eg, they reduce the requirement for the body to convert methionine into cysteine. Thus, although dietary methionine is essential for homoeostasis in adults and for regular development and advancement in children, dietary cysteine can reduce the daily methionine requirements.30 this impact is typically described as the sparing impact of cysteine on methionine requirement., the required minimum requirement for methionine intake in adults can be around 6 mg kg − 1d − 1.

The body maintains a balance in between synthesis and destruction of protein, and degradation of amino acids to acquire energy for the body’s needs. In particular, the liver is necessary for the body’s protein turnover. The liver’s regulative functions include the synthesis of non-essential amino acids, conversion of glucogenic amino acids to glucose or ketogenic amino acids to lipids, conversion of ammonia into urea, and the synthesis of a lot of plasma proteins. A nutritionally sufficient diet plan can be guaranteed by consuming a large range of protein (10– 35% of total energy intake for grownups and 5– 10 % for children). Protein intake of 0 · 66 g kg − 1d − 1 of balanced protein suffices for an average grownup. On average, human beings have around 150 g protein per kg of bodyweight.35 whole-body protein turnover in humans is relatively fast, with a typical protein synthesis rate approximated at around 4 g protein kg − 1d − 1 in the lack of net growth. The average half-life of the overall protein in human beings is most likely on the order of 80 days. We likewise presume that body methionine readily equilibrates for the most part with dietary consumption, however long-lived proteins and tissues do exist. Assuming an uniform turnover of methionine with very first order kinetics, it would be anticipated that within 2 years more than 80% of methionine in the body is replenished with methionine used up from the diet (offered a methionine intake or loss of 10 mg kg − 1d − 1, and a methionine pool of 4 g/kg). [12]

Side effects

To assess the body’s reactions to methionine, researchers will give a single big dosage of this amino acid and observe the results.

This dosage is far larger than the recommended consumption, frequently around 45 mg/lb (100 mg/kg), or 6.8 grams for somebody who weighs 150 pounds (68 kgs).

This type of test has actually been carried out over 6,000 times, with primarily minor side effects. These minor side effects include lightheadedness, sleepiness and modifications in high blood pressure.

One major negative event occurred throughout among these tests, which led to the death of a specific with hypertension but health otherwise.

Nevertheless, it promises that an unexpected overdose of roughly 70 times the advised consumption caused the problems.

Overall, it appears that methionine is not particularly harmful in healthy people, other than at extremely high doses that would be virtually difficult to obtain through the diet plan.

Even though methionine is associated with the production of homocysteine, there is no proof that consumption within a common variety is dangerous for heart health.


Individuals following many kinds of diet plans will often surpass the advised minimum consumption of methionine. Negative effects in reaction to big doses are typically minor but might become unsafe at very high dosages. [13]


Although methionine was labeled as being the most poisonous amino acid in relation to development in animals, the proof in humans does not indicate major toxicity, except at extremely high levels of consumption. In spite of the function of methionine as a precursor of homocysteine, and the role of homocysteine in vascular damage and cardiovascular disease, there is no evidence that dietary consumption of methionine within sensible limits will cause cardiovascular damage. A single dose of 100 mg/kg body weight has been revealed to be safe, however this dosage has to do with 7 times the day-to-day requirement for sulfur amino acids, and duplicated usage for 1 wk was revealed to result in increased homocysteine levels. Daily doses of 250 mg (i.e., 4 mg/kg per day) are only 25% of the day-to-day requirement and have actually been revealed to be safe. Overall, the literature recommends that the single dosage which is usually given in the methionine loading test (100mg/kg/d) does not cause any serious complications, other than in the extreme case when a 10-fold excess of methionine appears to have been provided, and in patients who have schizophrenia or innate mistakes of sulfur amino acid metabolism, such as hypermethioninemia. [14]


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